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TRIM16

Gene
TRIM16
Protein
Tripartite motif-containing protein 16
Organism
Homo sapiens
Length
564 amino acids
Function
E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage.
Similarity
Belongs to the TRIM/RBCC family.
Mass
63.955 kDa
Sequence
MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDSAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAWYSDMETPLKAGPFRRLGVYIDFPGGILSFYGVEYDTMTLVHKFACKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAPSLVGTAP

Gene
TRIM16
Protein
E3 ubiquitin-protein ligase TRIM16
Organism
Pongo abelii
Length
564 amino acids
Function
E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage.
Similarity
Belongs to the TRIM/RBCC family.
Mass
63.965 kDa
Sequence
MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDPAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAWYSDMETPLKAGPFRRLGVYIDFPGGILSFYGVEYDTMTLVHKFACKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAPSLVGTAP

Gene
Trim16
Protein
Tripartite motif-containing protein 16
Organism
Mus musculus
Length
556 amino acids
Function
E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage.
Similarity
Belongs to the TRIM/RBCC family.
Mass
62.943 kDa
Sequence
MAELDLIAPGPLTGVTAHPLAPLGPDPVSAIPVEKEDADPLSKSGEETQEQGHDPAELGAPGEEDQILCDFCLGASRVRAVKSCLTCMVNYCEEHLRPHQENSKLHSHQLTEPAKDQDLRTCPAHHSPLVSFCHTHQQCICQECGEGEHRGDSTVSLDAARRNKEVDLRCMQLDLEQKLKLNENAIARLQANHKSVLVSVSEVKVVAEEKFGELLAAVRKAQADVMVFLEEKEQAALNQVNSIKTHLEHRSLEMEKSKQELERLAAISNTVLFLEEYCKLKKTEDTASPSIYIGLKDKLSGIRKVITDSTLNLIQLLESYKEKLQEFSREEEYDIRTQVSAIVQRKYRTSKPEPRTRDEFLQYACDITFDPDTAHRYLRLQEDNRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVELSGGGTYVGLTCKGIDRKGEERNSCISGNSFSWSIHWNGKEFTAWHSDTETPLKVSPFRRLGIYVNFPGGILSFYGVEYDAMTLIHKFDCKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAGSSVEAAP